PA2_HOTTA
ID PA2_HOTTA Reviewed; 167 AA.
AC Q6T178;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Phospholipase A2;
DE Short=MtsPLA2;
DE Contains:
DE RecName: Full=Large subunit;
DE EC=3.1.1.4;
DE Contains:
DE RecName: Full=Small subunit;
DE Flags: Precursor;
OS Hottentotta tamulus (Eastern Indian scorpion) (Mesobuthus tamulus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Mesobuthus.
OX NCBI_TaxID=34647;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Venom gland;
RA Hariprasad R.G., Saravanan K., Singh S.B., Das U., Sharma S., Kaur P.,
RA Singh T.P., Srinivasan A.;
RT "Group III PLA2 from the scorpion, Mesobuthus tamulus: cloning and
RT recombinant expression in E. coli.";
RL Electron. J. Biotechnol. 12:1-6(2009).
RN [2]
RP 3D-STRUCTURE MODELING.
RX PubMed=21238479; DOI=10.1016/j.ijbiomac.2011.01.004;
RA Hariprasad G., Kumar M., Srinivasan A., Kaur P., Singh T.P., Jithesh O.;
RT "Structural analysis of a group III Glu62-phospholipase A2 from the
RT scorpion, Mesobuthus tamulus: targeting and reversible inhibition by native
RT peptides.";
RL Int. J. Biol. Macromol. 48:423-431(2011).
CC -!- FUNCTION: Phospholipase toxin, which catalyzes the calcium-dependent
CC hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Inhibits
CC both skeletal (RYR1) and cardiac (RYR2) ryanodine receptors (calcium
CC release channels). Probably blocks ryanodine receptors by generating a
CC lipid product (By similarity). Shows hemolytic activity, but it is not
CC know if it is direct or indirect. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10035};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|Ref.1};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000269|Ref.1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|Ref.1};
CC -!- SUBUNIT: Heterodimer composed of a large subunit and a small subunit;
CC disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group III
CC subfamily. {ECO:0000305}.
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DR EMBL; AY443497; AAR16429.1; -; mRNA.
DR AlphaFoldDB; Q6T178; -.
DR SMR; Q6T178; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005246; F:calcium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR Pfam; PF05826; Phospholip_A2_2; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW Calcium; Calcium channel impairing toxin; Disulfide bond; Glycoprotein;
KW Hydrolase; Ion channel impairing toxin; Lipid degradation;
KW Lipid metabolism; Metal-binding; Neurotoxin;
KW Ryanodine-sensitive calcium-release channel impairing toxin; Secreted;
KW Signal; Toxin; Zymogen.
FT SIGNAL 1..?
FT /evidence="ECO:0000250"
FT PROPEP ?..31
FT /evidence="ECO:0000250"
FT /id="PRO_0000429187"
FT CHAIN 32..135
FT /note="Large subunit"
FT /evidence="ECO:0000250"
FT /id="PRO_0000429188"
FT PROPEP 136..140
FT /evidence="ECO:0000250"
FT /id="PRO_0000429189"
FT CHAIN 141..167
FT /note="Small subunit"
FT /evidence="ECO:0000250"
FT /id="PRO_0000429190"
FT ACT_SITE 64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10035"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00630"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..61
FT /evidence="ECO:0000305|PubMed:21238479"
FT DISULFID 60..99
FT /evidence="ECO:0000305|PubMed:21238479"
FT DISULFID 67..92
FT /evidence="ECO:0000305|PubMed:21238479"
FT DISULFID 90..127
FT /evidence="ECO:0000305|PubMed:21238479"
FT DISULFID 132..144
FT /note="Interchain (between large and small subunits)"
FT /evidence="ECO:0000305|PubMed:21238479"
SQ SEQUENCE 167 AA; 18573 MW; 6FAF86D55B287A56 CRC64;
MHTPKHAIRR MSKGEMEFFE GRCQRMGEAK RTMWGTKWCG SGNEAINYTD LGYFSNLDSC
CRTHDHCDSI PAGETKYGLT NEGKYTMMNC KCESAFEKCL RDVRGILEGK AAAAVRKTYF
DLYGNGCFNV KCPSGARSAR SEECTNGMAT YTGETGYGAW AINKLNG
